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・ 3-hydroxyacyl-coenzyme A dehydrogenase deficiency
・ 3-hydroxyanthranilate 3,4-dioxygenase
・ 3-hydroxyanthranilate 4-C-methyltransferase
・ 3-hydroxyanthranilate oxidase
・ 3-Hydroxyanthranilic acid
・ 3-hydroxyaspartate aldolase
・ 3-Hydroxyaspartic acid
・ 3-Hydroxybenzaldehyde
・ 3-hydroxybenzoate 2-monooxygenase
・ 3-hydroxybenzoate 4-monooxygenase
・ 3-hydroxybenzoate 6-monooxygenase
・ 3-hydroxybenzoate—CoA ligase
・ 3-Hydroxybenzoic acid
・ 3-hydroxybenzyl-alcohol dehydrogenase
・ 3-Hydroxybutanal
3-hydroxybutyrate dehydrogenase
・ 3-hydroxybutyryl-CoA dehydratase
・ 3-hydroxybutyryl-CoA dehydrogenase
・ 3-hydroxybutyryl-CoA epimerase
・ 3-hydroxycyclohexanone dehydrogenase
・ 3-hydroxydecanoyl-(acyl-carrier-protein) dehydratase
・ 3-Hydroxyflavone
・ 3-hydroxyindolin-2-one monooxygenase
・ 3-hydroxyisobutyrate dehydrogenase
・ 3-Hydroxyisobutyric acid
・ 3-Hydroxyisobutyryl-CoA
・ 3-hydroxyisobutyryl-CoA hydrolase
・ 3-Hydroxykynurenine
・ 3-hydroxymethylcephem carbamoyltransferase
・ 3-Hydroxymorphinan


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3-hydroxybutyrate dehydrogenase : ウィキペディア英語版
3-hydroxybutyrate dehydrogenase

In enzymology, a 3-hydroxybutyrate dehydrogenase () is an enzyme that catalyzes the chemical reaction
:(''R'')-3-hydroxybutanoate + NAD+ \rightleftharpoons acetoacetate + NADH + H+
Thus, the two substrates of this enzyme are (''R'')-3-hydroxybutanoate and NAD+, whereas its three products are acetoacetate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (''R'')-3-hydroxybutanoate:NAD+ oxidoreductase. Other names in common use include NAD+-''beta''-hydroxybutyrate dehydrogenase, hydroxybutyrate oxidoreductase, ''beta''-hydroxybutyrate dehydrogenase, D-''beta''-hydroxybutyrate dehydrogenase, D-3-hydroxybutyrate dehydrogenase, D-(–)-3-hydroxybutyrate dehydrogenase, ''beta''-hydroxybutyric acid dehydrogenase, 3-D-hydroxybutyrate dehydrogenase, and ''beta''-hydroxybutyric dehydrogenase. This enzyme participates in synthesis and degradation of ketone bodies and butanoate metabolism.
== Structural studies ==

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .

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